Journal:Acta Cryst F:S2053230X23004430
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<scene name='96/967852/Homotetramer/3'>The ALDHSt homotetramer</scene> is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. <scene name='96/967852/Monomer/1'>Structure of the monomer subunit</scene>. The cofactor-binding domain, catalytic domain and oligomerization domain are shown in green, cyan and magenta, respectively. NADP is shown as a yellow stick model. | <scene name='96/967852/Homotetramer/3'>The ALDHSt homotetramer</scene> is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. <scene name='96/967852/Monomer/1'>Structure of the monomer subunit</scene>. The cofactor-binding domain, catalytic domain and oligomerization domain are shown in green, cyan and magenta, respectively. NADP is shown as a yellow stick model. | ||
| - | <scene name='96/967852/Binding_site/3'>Coenzyme NADP binding site</scene>. NADP and NADP-interacting residues are shown in ball-and-stick representation, water molecules are shown as red spheres. Hydrogen bonds are shown as dashed lines. <scene name='96/967852/Catalytic_residues/2'>The catalytic residues Asn142, Glu240, Cys274, Glu370 and Phe372</scene> | + | <scene name='96/967852/Binding_site/3'>Coenzyme NADP binding site</scene>. NADP and NADP-interacting residues are shown in ball-and-stick representation, water molecules are shown as red spheres. Hydrogen bonds are shown as dashed lines. <scene name='96/967852/Catalytic_residues/2'>The catalytic residues Asn142, Glu240, Cys274, Glu370 and Phe372</scene> (colored in deep pink). <scene name='96/967852/Asn142/1'>The conformation of the active-site residue Asn142 in ALDHSt</scene>. An omit F<sub>o</sub> - F<sub>c</sub> electron-density map for ligands was observed between the side chains of Asn142 and Cys274. This space appeared to be the binding-site cleft for the substrate. Therefore, we propose the involvement of the amide group of the side chain of Asn142 in an oxyanion hole to stabilize the reaction intermediate, as suggested previously. Arg88 and Phe143 were also observed near this site, but were not conserved in ALDH. |
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| + | <scene name='96/967852/Salt_bridges/2'>The surface structure of the alpha-helices in the cofactor-binding domain of ALDHSt</scene>. <span class="bg-yellow"><span class="far fa-hand-point-right"></span> Remember to drag the structures with the mouse to rotate them.</span> Arg, Glu and Asp residues involved in salt bridges are shown as ball-and-stick models with the interactions shown as dashed lines on the alpha-helix structures in the cofactor-binding domain of ALDHSt. | ||
<b>References</b><br> | <b>References</b><br> | ||
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